ID A0A6I8RT08_XENTR Unreviewed; 632 AA.
AC A0A6I8RT08; A0A6I8S017;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Poly(A)-specific ribonuclease PARN {ECO:0000256|ARBA:ARBA00015918};
DE EC=3.1.13.4 {ECO:0000256|ARBA:ARBA00012161};
DE AltName: Full=Polyadenylate-specific ribonuclease {ECO:0000256|ARBA:ARBA00031923};
GN Name=parn {ECO:0000313|Ensembl:ENSXETP00000083713,
GN ECO:0000313|RefSeq:XP_012825962.2,
GN ECO:0000313|Xenbase:XB-GENE-1003103};
GN Synonyms=xparn {ECO:0000313|RefSeq:XP_012825962.2};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000083713};
RN [1] {ECO:0000313|Ensembl:ENSXETP00000083713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000083713};
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2] {ECO:0000313|Ensembl:ENSXETP00000083713}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAY-2020) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:XP_012825962.2}
RP IDENTIFICATION.
RC STRAIN=Nigerian {ECO:0000313|RefSeq:XP_012825962.2};
RC TISSUE=Liver and blood {ECO:0000313|RefSeq:XP_012825962.2};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
CC Evidence={ECO:0000256|ARBA:ARBA00001663};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the CAF1 family.
CC {ECO:0000256|ARBA:ARBA00008372}.
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DR RefSeq; XP_012825962.2; XM_012970508.3.
DR Ensembl; ENSXETT00000083144; ENSXETP00000083713; ENSXETG00000010994.
DR Ensembl; ENSXETT00000099576; ENSXETP00000088272; ENSXETG00000010994.
DR Xenbase; XB-GENE-1003103; parn.
DR OMA; LTTCHED; -.
DR Reactome; R-XTR-429947; Deadenylation of mRNA.
DR Reactome; R-XTR-450604; KSRP (KHSRP) binds and destabilizes mRNA.
DR Proteomes; UP000008143; Chromosome 9.
DR Bgee; ENSXETG00000010994; Expressed in ovary and 13 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:InterPro.
DR CDD; cd02637; R3H_PARN; 1.
DR CDD; cd12428; RRM_PARN; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR034042; PARN_R3H.
DR InterPro; IPR014789; PolyA-riboNase_RNA-binding.
DR InterPro; IPR001374; R3H_dom.
DR InterPro; IPR036867; R3H_dom_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR006941; RNase_CAF1.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR15092; POLY A -SPECIFIC RIBONUCLEASE/TARGET OF EGR1, MEMBER 1; 1.
DR PANTHER; PTHR15092:SF44; POLY(A)-SPECIFIC RIBONUCLEASE PARN; 1.
DR Pfam; PF04857; CAF1; 1.
DR Pfam; PF01424; R3H; 1.
DR Pfam; PF08675; RNA_bind; 1.
DR SUPFAM; SSF82708; R3H domain; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS51061; R3H; 1.
PE 3: Inferred from homology;
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Reference proteome {ECO:0000313|Proteomes:UP000008143}.
FT DOMAIN 178..244
FT /note="R3H"
FT /evidence="ECO:0000259|PROSITE:PS51061"
FT REGION 145..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 632 AA; 72970 MW; 591EBCFFAE1E9898 CRC64;
MEMTRSNFKD NLPKVYKAIE EADFLAIDGE FSGISDGPSV STLTNGFDTP EERYTKLKKH
SMEFLLFQFG LCTFNYDNTE AKYFMKSFNF YIFPKPFNRN SPDKKFVCQS SSIDFLANQG
FDFNKVFRNG IPYLNQEEEK QLRDQYEERR SQSNGASAMS YVSPNASKTP VSIPDEQKGF
IDKVVERVED FLKNEQKSMD VEPCTGYQRK LIYQTLNWKY PRGIHVETLE SEKKERYIVI
SKVDEEERKR MEQQKQAKER EELDDAVGFS RIIQAISSSG KLVVGHNMLL DIMHTIHQFF
CQLPDELNEF KEVTNCVFPR VLDTKLMAST NPFKEIIYNT SLAELEKRLK EAPFKPPKVD
SAEGFPSYNT ASEQLHEAGY DAYITGLCFI SMANYLGSFL SPPKGYVSSR SKIIRPFFNK
LFLMRIMDIP YLNLEGPDLQ PKRDNVLHVA FPKEWKTSDL YQLFSAFGNI QVSWIDDTSA
FVSLSHPDQV QIAVNTSKYA ESYRIQTYAE YVEKKNEENQ TKRKWAEDGW KDLERKRLKT
QYNSYIPQTP VFYGNCFVAP SYAVKRSMSP IQEETASENT EEVRAQEDDP SNPGATEQGK
KPKNHKRQKT DSTPPETSDS GSSVLFEVPD TW
//
